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Methods of producing a recombinant polypeptide in a filamentous fungus

IP.com Disclosure Number: IPCOM000244485D
Publication Date: 2015-Dec-16
Document File: 301 page(s) / 1M

Publishing Venue

The IP.com Prior Art Database

Abstract

The present Publication relates to a two methods of producing a recombinant polypeptide in a filamentous fungus which is genetically modified to decrease or eliminate the activity of CLR1 (Part 1) or CLR2 (Part 2) and to express said recombinant polypeptides. The method further relates to a filamentous fungus Myceliophthora thermophila, which is genetically modified to decrease or eliminate the activity of CLR1 or CLR2 and to the use of this filamentous fungus in the production of a recombinant polypeptide.

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A B S T R A C T

The present Publication relates to a two methods of producing a recombinant polypeptide in a filamentous fungus which is genetically modified to decrease or eliminate the activity of

CLR1 (Part 1) or CLR2 (Part 2) and to express said recombinant polypeptides.

The method further relates to a filamentous fungus Myceliophthora thermophila, which is genetically modified to decrease or eliminate the activity of CLR1 or CLR2 and to the use of this filamentous fungus in the production of a recombinant polypeptide.

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Part 1:


Method of producing proteins in filamentous fungi with decreased CLR1 activity

   FIELD OF THE PUBLICATION 5

The present Publication relates to a method of producing a recombinant polypeptide in a filamentous fungus which is genetically modified to decrease or eliminate the activity of CLR1 and to express said recombinant polypeptide. The method further relates to a filamentous fungus Myceliophthora thermophila, which is genetically modified to decrease or eliminate the activity of CLR1 and to the use of this filamentous fungus in the production of a

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recombinant polypeptide.

BACKGROUND

Filamentous fungi have been shown to be excellent hosts for the production of a variety of

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proteins. Fungal strains such as Aspergillus, Trichoderma, Penicillium and Myceliophthora have been applied in the industrial production of a wide range of enzymes, since they can secrete large amounts of protein into the fermentation broth. The protein-secreting capacity of these fungi makes them preferred hosts for the targeted production of specific enzymes or enzyme mixtures. However, typically, these hosts secrete a mixture of many different

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enzymes, making the crude protein product undefined and requiring complex purification schemes for the desired protein. Even in cases where the gene encoding the target enzyme is overexpressed by genetic modification, the target enzyme will only constitute a minor part of the total secreted protein.

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Hence, it is highly desirable to provide a fungal production system which is able to secrete high amounts of a specific enzyme without the presence of high levels of other proteins.

Such a production system would enable the production of a relatively pure enzyme and a simplified large scale purification of the desired enzyme. The produced enzyme can be used

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for different applications, e.g. for food and feed applications, in detergents and home care as well as in plant biomass hydrolysis (biofuels and chemicals), textile finishing and in paper and pulp industry.

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WO 2010/107303 A2 describes the UV-induced mutagenesis of a Myceliophthora thermophila strain leading to isolates which produce low amounts of endogenous cellulase and proteases. Visser et al. (2011) Industrial Biotechnology 7(3): 214-223 disclose a Myceliophthora thermophila strain called LC (low-cellulase) strain which has lost almost all of its ability to produce cellulase....